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Q15025

- TNIP1_HUMAN

UniProt

Q15025 - TNIP1_HUMAN

Protein

TNFAIP3-interacting protein 1

Gene

TNIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Aug 1999)
      Previous versions | rss
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    Functioni

    Inhibits NF-kappa-B activation and TNF-induced NF-kappa-B-dependent gene expression by regulating A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG. Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcription. Increases cell surface CD4(T4) antigen expression. Involved in the anti-inflammatory response of macrophages and positively regulates TLR-induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflammation; this function is mediated by association with SELPLG and dependent on phosphorylation by SRC-family kinases. Interacts with HIV-1 matrix protein and is packaged into virions and overexpression can inhibit viral replication. May regulate matrix nuclear localization, both nuclear import of PIC (Preintegration complex) and export of GAG polyprotein and viral genomic RNA during virion production. In case of infection, promotes association of IKBKG with Shigella flexneri E3 ubiquitin-protein ligase ipah9.8 p which in turn promotes polyubiquitination of IKBKG leading to its proteasome-dependent degradation and thus is perturbing NF-kappa-B activation during bacterial infection.5 Publications

    GO - Molecular functioni

    1. mitogen-activated protein kinase binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. defense response Source: ProtInc
    2. glycoprotein biosynthetic process Source: UniProtKB
    3. inflammatory response Source: UniProtKB-KW
    4. leukocyte cell-cell adhesion Source: UniProtKB
    5. modulation by symbiont of host I-kappaB kinase/NF-kappaB cascade Source: UniProtKB
    6. MyD88-dependent toll-like receptor signaling pathway Source: UniProtKB
    7. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
    8. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    9. negative regulation of viral genome replication Source: UniProtKB
    10. positive regulation of inflammatory response Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    12. translation Source: ProtInc

    Keywords - Biological processi

    Inflammatory response

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TNFAIP3-interacting protein 1
    Alternative name(s):
    A20-binding inhibitor of NF-kappa-B activation 1
    Short name:
    ABIN-1
    HIV-1 Nef-interacting protein
    Nef-associated factor 1
    Short name:
    Naf1
    Nip40-1
    Virion-associated nuclear shuttling protein
    Short name:
    VAN
    Short name:
    hVAN
    Gene namesi
    Name:TNIP1
    Synonyms:KIAA0113, NAF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:16903. TNIP1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. intracellular Source: UniProtKB
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi472 – 4721D → N: Abolishes binding to polyubiquitin ('K-63'-linked and linear). 2 Publications
    Mutagenesisi552 – 5521Y → F: Abolishes interaction with PI3K p85 regulatory subunit and abolishes interaction between SELPLG and PI3K p85 regulatory subunit. 2 Publications

    Organism-specific databases

    Orphaneti536. Systemic lupus erythematosus.
    PharmGKBiPA128394573.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 636636TNFAIP3-interacting protein 1PRO_0000096691Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei403 – 4031Phosphoserine3 Publications
    Modified residuei438 – 4381Phosphothreonine1 Publication
    Modified residuei442 – 4421Phosphoserine1 Publication
    Modified residuei552 – 5521Phosphotyrosine1 Publication

    Post-translational modificationi

    Phosphorylation at Tyr-552 by SRC-family kinases recruits phosphoinositide-3-kinase (PI3K) PIK3CD:p85 heterodimer which results in integrin activation and leukocyte adhesion to activated endothelium during inflammation.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15025.
    PaxDbiQ15025.
    PRIDEiQ15025.

    PTM databases

    PhosphoSiteiQ15025.

    Expressioni

    Tissue specificityi

    Ubiquitous. Strongly expressed in peripheral blood lymphocytes, spleen and skeletal muscle, and is weakly expressed in the brain. In peripheral blood mononucleocytes, isoform 4 is mainly expressed and isoform 1 and isoform 7 are almost not expressed. Expression of isoform 1 and isoform 7 increases in leukemic cells.1 Publication

    Gene expression databases

    ArrayExpressiQ15025.
    BgeeiQ15025.
    CleanExiHS_NAF1.
    HS_TNIP1.
    GenevestigatoriQ15025.

    Organism-specific databases

    HPAiHPA037893.
    HPA037894.

    Interactioni

    Subunit structurei

    Interacts with TNFAIP3 and IKBKG (polyubiquitinated); facilitates TNFAIP3-mediated de-ubiquitination of NEMO/IKBKG. Interacts with polyubiquitin. Interacts with MAPK1, SELPLG and PIK3CD. Interacts with IRAK1 (polyubiquitinated). Interacts with MYD88; the interaction is indicative for participation in an activated TLR-signaling complex. Interacts with HIV-1 matrix protein. Interacts with Shigella flexneri ipah9.8; the interaction promotes polyubiquitination of IKBKG.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCNG1P519594EBI-357849,EBI-3905829
    GIT2Q141613EBI-357849,EBI-1046878
    IKBKGQ9Y6K94EBI-357849,EBI-81279
    ipaH9.8Q8VSC34EBI-357849,EBI-6125799From a different organism.
    MAGEB18Q96M612EBI-357849,EBI-741835
    OPTNQ96CV93EBI-357849,EBI-748974

    Protein-protein interaction databases

    BioGridi115602. 37 interactions.
    DIPiDIP-27577N.
    IntActiQ15025. 31 interactions.
    MINTiMINT-200912.
    STRINGi9606.ENSP00000317891.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15025.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni94 – 412319Interacts with NefAdd
    BLAST
    Regioni351 – 36717Interaction with Shigella flexneri ipah9.8Add
    BLAST
    Regioni431 – 588158Required for inhibitory activity of TNF-induced NF-kappa-B activationBy similarityAdd
    BLAST
    Regioni452 – 51059Ubiquitin-binding domain (UBD)Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili20 – 7354Sequence AnalysisAdd
    BLAST
    Coiled coili196 – 25863Sequence AnalysisAdd
    BLAST
    Coiled coili294 – 535242Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi524 – 5307Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi539 – 63698Pro-richAdd
    BLAST

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG120932.
    HOGENOMiHOG000253048.
    HOVERGENiHBG019072.
    InParanoidiQ15025.
    OMAiNQSSQVM.
    OrthoDBiEOG7SJD44.
    PhylomeDBiQ15025.
    TreeFamiTF351138.

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q15025-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha, FL

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEGRGPYRIY DPGGSVPSGE ASAAFERLVK ENSRLKEKMQ GIKMLGELLE    50
    ESQMEATRLR QKAEELVKDN ELLPPPSPSL GSFDPLAELT GKDSNVTASP 100
    TAPACPSDKP APVQKPPSSG TSSEFEVVTP EEQNSPESSS HANAMALGPL 150
    PREDGNLMLH LQRLETTLSV CAEEPDHGQL FTHLGRMALE FNRLASKVHK 200
    NEQRTSILQT LCEQLRKENE ALKAKLDKGL EQRDQAAERL REENLELKKL 250
    LMSNGNKEGA SGRPGSPKME GTGKKAVAGQ QQASVTAGKV PEVVALGAAE 300
    KKVKMLEQQR SELLEVNKQW DQHFRSMKQQ YEQKITELRQ KLADLQKQVT 350
    DLEAEREQKQ RDFDRKLLLA KSKIEMEETD KEQLTAEAKE LRQKVKYLQD 400
    QLSPLTRQRE YQEKEIQRLN KALEEALSIQ TPPSSPPTAF GSPEGAGALL 450
    RKQELVTQNE LLKQQVKIFE EDFQRERSDR ERMNEEKEEL KKQVEKLQAQ 500
    VTLSNAQLKA FKDEEKAREA LRQQKRKAKA SGERYHVEPH PEHLCGAYPY 550
    AYPPMPAMVP HHGFEDWSQI RYPPPPMAME HPPPLPNSRL FHLPEYTWRL 600
    PCGGVRNPNQ SSQVMDPPTA RPTEPESPKN DREGPQ 636
    Length:636
    Mass (Da):71,864
    Last modified:August 1, 1999 - v2
    Checksum:iD81B96BEAD50D871
    GO
    Isoform 2 (identifier: Q15025-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         627-636: SPKNDREGPQ → PADLRLPRN

    Show »
    Length:635
    Mass (Da):71,788
    Checksum:iFE65D2CE6E7B185B
    GO
    Isoform 3 (identifier: Q15025-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: Missing.

    Show »
    Length:583
    Mass (Da):66,012
    Checksum:iA97F0EB85F9F39DE
    GO
    Isoform 4 (identifier: Q15025-4) [UniParc]FASTAAdd to Basket

    Also known as: Alpha2

    The sequence of this isoform differs from the canonical sequence as follows:
         530-593: Missing.

    Show »
    Length:572
    Mass (Da):64,500
    Checksum:iD1E76C1FBBA59E63
    GO
    Isoform 5 (identifier: Q15025-5) [UniParc]FASTAAdd to Basket

    Also known as: Alpha4

    The sequence of this isoform differs from the canonical sequence as follows:
         530-556: ASGERYHVEPHPEHLCGAYPYAYPPMP → SLQKMTVRGLSETRLCHLAPPSSCRAS
         557-636: Missing.

    Note: Less effective in the NF-kappa-B inhibitory effect.

    Show »
    Length:556
    Mass (Da):62,609
    Checksum:i757B3E9B83C35F42
    GO
    Isoform 6 (identifier: Q15025-6) [UniParc]FASTAAdd to Basket

    Also known as: Beta2

    The sequence of this isoform differs from the canonical sequence as follows:
         530-593: Missing.
         627-636: SPKNDREGPQ → PADLRLPRN

    Show »
    Length:571
    Mass (Da):64,424
    Checksum:i929F73D89B3D0A54
    GO
    Isoform 7 (identifier: Q15025-7) [UniParc]FASTAAdd to Basket

    Also known as: Alpha3, Beta3

    The sequence of this isoform differs from the canonical sequence as follows:
         530-545: ASGERYHVEPHPEHLC → GTHRGCPRRLPERKVK
         546-636: Missing.

    Show »
    Length:545
    Mass (Da):61,570
    Checksum:i7F4AD5363F28608B
    GO
    Isoform 8 (identifier: Q15025-8) [UniParc]FASTAAdd to Basket

    Also known as: Beta4

    The sequence of this isoform differs from the canonical sequence as follows:
         530-552: ASGERYHVEPHPEHLCGAYPYAY → SQLISDCQETRSHLHGVARASAG
         553-636: Missing.

    Show »
    Length:552
    Mass (Da):62,103
    Checksum:i699AD04365381366
    GO

    Sequence cautioni

    The sequence AAB41438.1 differs from that shown. Reason: Frameshift at positions 152 and 154.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti148 – 1481G → D in AAH12133. (PubMed:15489334)Curated
    Sequence conflicti178 – 1781G → S in BAH13185. (PubMed:14702039)Curated
    Sequence conflicti299 – 2991A → P in AAG42154. (PubMed:11090181)Curated
    Sequence conflicti299 – 2991A → P in BAF34946. (PubMed:17016622)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031P → S.
    Corresponds to variant rs2303018 [ dbSNP | Ensembl ].
    VAR_051453
    Natural varianti146 – 1461A → V.
    Corresponds to variant rs2233289 [ dbSNP | Ensembl ].
    VAR_051454
    Natural varianti151 – 1511P → A.
    Corresponds to variant rs2233290 [ dbSNP | Ensembl ].
    VAR_051455
    Natural varianti233 – 2331R → Q.
    Corresponds to variant rs2233292 [ dbSNP | Ensembl ].
    VAR_051456
    Natural varianti260 – 2601A → V.
    Corresponds to variant rs2233295 [ dbSNP | Ensembl ].
    VAR_051457
    Natural varianti263 – 2631R → W in patients with gastrointestinal diffuse large cell lymphoma. 1 Publication
    Corresponds to variant rs117663772 [ dbSNP | Ensembl ].
    VAR_067965
    Natural varianti286 – 2861T → M in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation. 1 Publication
    Corresponds to variant rs185683917 [ dbSNP | Ensembl ].
    VAR_067966
    Natural varianti374 – 3741I → T in patients with gastrointestinal diffuse large cell lymphoma. 1 Publication
    VAR_067967
    Natural varianti476 – 4761E → K in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation; loss of inhibitory activity on CARD11- and TNF-induced NF-kappa-B activation. 1 Publication
    VAR_067968

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5353Missing in isoform 3. 3 PublicationsVSP_045296Add
    BLAST
    Alternative sequencei530 – 59364Missing in isoform 4 and isoform 6. 1 PublicationVSP_055208Add
    BLAST
    Alternative sequencei530 – 55627ASGER…YPPMP → SLQKMTVRGLSETRLCHLAP PSSCRAS in isoform 5. 1 PublicationVSP_055209Add
    BLAST
    Alternative sequencei530 – 55223ASGER…YPYAY → SQLISDCQETRSHLHGVARA SAG in isoform 8. 1 PublicationVSP_055210Add
    BLAST
    Alternative sequencei530 – 54516ASGER…PEHLC → GTHRGCPRRLPERKVK in isoform 7. 1 PublicationVSP_055211Add
    BLAST
    Alternative sequencei546 – 63691Missing in isoform 7. 1 PublicationVSP_055212Add
    BLAST
    Alternative sequencei553 – 63684Missing in isoform 8. 1 PublicationVSP_055213Add
    BLAST
    Alternative sequencei557 – 63680Missing in isoform 5. 1 PublicationVSP_055214Add
    BLAST
    Alternative sequencei627 – 63610SPKNDREGPQ → PADLRLPRN in isoform 2 and isoform 6. 3 PublicationsVSP_003913

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011895 mRNA. Translation: CAA09855.1.
    AJ011896 mRNA. Translation: CAA09856.1.
    AY012155 mRNA. Translation: AAG42154.1.
    AB177543 mRNA. Translation: BAF34946.1.
    AB177544 mRNA. Translation: BAF34947.1.
    AB252970 mRNA. Translation: BAF48787.1.
    AB252971 mRNA. Translation: BAF48788.1.
    AB252972 mRNA. Translation: BAF48789.1.
    AB252973 mRNA. Translation: BAF48790.1.
    AB252974 mRNA. Translation: BAF48791.1.
    AB252975 mRNA. Translation: BAF48792.1.
    AB252976 mRNA. Translation: BAF48793.1.
    AB252977 mRNA. Translation: BAF48794.1.
    AB252978 mRNA. Translation: BAF48795.1.
    AB252979 mRNA. Translation: BAF48796.1.
    AB252980 mRNA. Translation: BAF48797.1.
    AB252981 mRNA. Translation: BAF48798.1.
    D30755 mRNA. Translation: BAA06416.2.
    AK299975 mRNA. Translation: BAH13185.1.
    BX640647 mRNA. Translation: CAE45793.1.
    AC008641 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61688.1.
    CH471062 Genomic DNA. Translation: EAW61689.1.
    CH471062 Genomic DNA. Translation: EAW61690.1.
    CH471062 Genomic DNA. Translation: EAW61691.1.
    BC012133 mRNA. Translation: AAH12133.1.
    BC014008 mRNA. Translation: AAH14008.1.
    U39403 mRNA. Translation: AAC99999.1.
    U83844 mRNA. Translation: AAB41438.1. Frameshift.
    CCDSiCCDS34280.1. [Q15025-1]
    CCDS58982.1. [Q15025-3]
    CCDS58983.1. [Q15025-5]
    CCDS58984.1. [Q15025-4]
    CCDS58985.1. [Q15025-2]
    RefSeqiNP_001239314.1. NM_001252385.1.
    NP_001239315.1. NM_001252386.1. [Q15025-3]
    NP_001239319.1. NM_001252390.1. [Q15025-1]
    NP_001239320.1. NM_001252391.1. [Q15025-1]
    NP_001239321.1. NM_001252392.1. [Q15025-2]
    NP_001239322.1. NM_001252393.1. [Q15025-2]
    NP_001245383.1. NM_001258454.1. [Q15025-1]
    NP_001245384.1. NM_001258455.1.
    NP_001245385.1. NM_001258456.1.
    NP_006049.3. NM_006058.4. [Q15025-1]
    XP_006714814.1. XM_006714751.1.
    XP_006714815.1. XM_006714752.1.
    UniGeneiHs.355141.
    Hs.731557.

    Genome annotation databases

    EnsembliENST00000315050; ENSP00000317891; ENSG00000145901. [Q15025-1]
    ENST00000389378; ENSP00000374029; ENSG00000145901. [Q15025-1]
    ENST00000518977; ENSP00000430971; ENSG00000145901. [Q15025-2]
    ENST00000520931; ENSP00000429891; ENSG00000145901. [Q15025-3]
    ENST00000521591; ENSP00000430760; ENSG00000145901. [Q15025-1]
    ENST00000522226; ENSP00000428187; ENSG00000145901. [Q15025-1]
    ENST00000523200; ENSP00000431105; ENSG00000145901. [Q15025-4]
    ENST00000523338; ENSP00000428243; ENSG00000145901. [Q15025-2]
    ENST00000524280; ENSP00000429912; ENSG00000145901. [Q15025-5]
    GeneIDi10318.
    KEGGihsa:10318.
    UCSCiuc003ltg.4. human. [Q15025-1]

    Polymorphism databases

    DMDMi20138952.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011895 mRNA. Translation: CAA09855.1 .
    AJ011896 mRNA. Translation: CAA09856.1 .
    AY012155 mRNA. Translation: AAG42154.1 .
    AB177543 mRNA. Translation: BAF34946.1 .
    AB177544 mRNA. Translation: BAF34947.1 .
    AB252970 mRNA. Translation: BAF48787.1 .
    AB252971 mRNA. Translation: BAF48788.1 .
    AB252972 mRNA. Translation: BAF48789.1 .
    AB252973 mRNA. Translation: BAF48790.1 .
    AB252974 mRNA. Translation: BAF48791.1 .
    AB252975 mRNA. Translation: BAF48792.1 .
    AB252976 mRNA. Translation: BAF48793.1 .
    AB252977 mRNA. Translation: BAF48794.1 .
    AB252978 mRNA. Translation: BAF48795.1 .
    AB252979 mRNA. Translation: BAF48796.1 .
    AB252980 mRNA. Translation: BAF48797.1 .
    AB252981 mRNA. Translation: BAF48798.1 .
    D30755 mRNA. Translation: BAA06416.2 .
    AK299975 mRNA. Translation: BAH13185.1 .
    BX640647 mRNA. Translation: CAE45793.1 .
    AC008641 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61688.1 .
    CH471062 Genomic DNA. Translation: EAW61689.1 .
    CH471062 Genomic DNA. Translation: EAW61690.1 .
    CH471062 Genomic DNA. Translation: EAW61691.1 .
    BC012133 mRNA. Translation: AAH12133.1 .
    BC014008 mRNA. Translation: AAH14008.1 .
    U39403 mRNA. Translation: AAC99999.1 .
    U83844 mRNA. Translation: AAB41438.1 . Frameshift.
    CCDSi CCDS34280.1. [Q15025-1 ]
    CCDS58982.1. [Q15025-3 ]
    CCDS58983.1. [Q15025-5 ]
    CCDS58984.1. [Q15025-4 ]
    CCDS58985.1. [Q15025-2 ]
    RefSeqi NP_001239314.1. NM_001252385.1.
    NP_001239315.1. NM_001252386.1. [Q15025-3 ]
    NP_001239319.1. NM_001252390.1. [Q15025-1 ]
    NP_001239320.1. NM_001252391.1. [Q15025-1 ]
    NP_001239321.1. NM_001252392.1. [Q15025-2 ]
    NP_001239322.1. NM_001252393.1. [Q15025-2 ]
    NP_001245383.1. NM_001258454.1. [Q15025-1 ]
    NP_001245384.1. NM_001258455.1.
    NP_001245385.1. NM_001258456.1.
    NP_006049.3. NM_006058.4. [Q15025-1 ]
    XP_006714814.1. XM_006714751.1.
    XP_006714815.1. XM_006714752.1.
    UniGenei Hs.355141.
    Hs.731557.

    3D structure databases

    ProteinModelPortali Q15025.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115602. 37 interactions.
    DIPi DIP-27577N.
    IntActi Q15025. 31 interactions.
    MINTi MINT-200912.
    STRINGi 9606.ENSP00000317891.

    PTM databases

    PhosphoSitei Q15025.

    Polymorphism databases

    DMDMi 20138952.

    Proteomic databases

    MaxQBi Q15025.
    PaxDbi Q15025.
    PRIDEi Q15025.

    Protocols and materials databases

    DNASUi 10318.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315050 ; ENSP00000317891 ; ENSG00000145901 . [Q15025-1 ]
    ENST00000389378 ; ENSP00000374029 ; ENSG00000145901 . [Q15025-1 ]
    ENST00000518977 ; ENSP00000430971 ; ENSG00000145901 . [Q15025-2 ]
    ENST00000520931 ; ENSP00000429891 ; ENSG00000145901 . [Q15025-3 ]
    ENST00000521591 ; ENSP00000430760 ; ENSG00000145901 . [Q15025-1 ]
    ENST00000522226 ; ENSP00000428187 ; ENSG00000145901 . [Q15025-1 ]
    ENST00000523200 ; ENSP00000431105 ; ENSG00000145901 . [Q15025-4 ]
    ENST00000523338 ; ENSP00000428243 ; ENSG00000145901 . [Q15025-2 ]
    ENST00000524280 ; ENSP00000429912 ; ENSG00000145901 . [Q15025-5 ]
    GeneIDi 10318.
    KEGGi hsa:10318.
    UCSCi uc003ltg.4. human. [Q15025-1 ]

    Organism-specific databases

    CTDi 10318.
    GeneCardsi GC05M150409.
    HGNCi HGNC:16903. TNIP1.
    HPAi HPA037893.
    HPA037894.
    MIMi 607714. gene.
    neXtProti NX_Q15025.
    Orphaneti 536. Systemic lupus erythematosus.
    PharmGKBi PA128394573.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG120932.
    HOGENOMi HOG000253048.
    HOVERGENi HBG019072.
    InParanoidi Q15025.
    OMAi NQSSQVM.
    OrthoDBi EOG7SJD44.
    PhylomeDBi Q15025.
    TreeFami TF351138.

    Miscellaneous databases

    ChiTaRSi TNIP1. human.
    GeneWikii TNIP1.
    GenomeRNAii 10318.
    NextBioi 35461715.
    PROi Q15025.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15025.
    Bgeei Q15025.
    CleanExi HS_NAF1.
    HS_TNIP1.
    Genevestigatori Q15025.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Identification and cloning of a novel cellular protein Naf1, Nef-associated factor 1, that increases cell surface CD4 expression."
      Fukushi M., Dixon J., Kimura T., Tsurutani N., Dixon M.J., Yamamoto N.
      FEBS Lett. 442:83-88(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Peripheral blood.
    2. "A human nuclear shuttling protein that interacts with human immunodeficiency virus type 1 matrix is packaged into virions."
      Gupta K., Ott D., Hope T.J., Siliciano R.F., Boeke J.D.
      J. Virol. 74:11811-11824(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Leukocyte.
    3. "Multiple splicing variants of Naf1/ABIN-1 transcripts and their alterations in hematopoietic tumors."
      Shiote Y., Ouchida M., Jitsumori Y., Ogama Y., Matsuo Y., Ishimaru F., Tanimoto M., Shimizu K.
      Int. J. Mol. Med. 18:917-923(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, FUNCTION.
    4. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
      DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Colon endothelium.
    8. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung.
    11. "Transcriptional map of the Treacher Collins candidate gene region."
      Loftus S.K., Dixon J., Koprivnikar K., Dixon M.J., Wasmuth J.J.
      Genome Res. 6:26-34(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-636 (ISOFORM 2).
      Tissue: Craniofacial.
    12. Fukushi M., Kimura T., Yamamoto N.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-412.
    13. Cited for: FUNCTION, INTERACTION WITH MAPK1.
    14. "ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting NF-kappaB."
      Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A., Acquaviva R., Formisano S., Vito P., Leonardi A.
      J. Biol. Chem. 281:18482-18488(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IKBKG AND TNFAIP3.
    15. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "P-selectin primes leukocyte integrin activation during inflammation."
      Wang H.B., Wang J.T., Zhang L., Geng Z.H., Xu W.L., Xu T., Huo Y., Zhu X., Plow E.F., Chen M., Geng J.G.
      Nat. Immunol. 8:882-892(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SELPLG AND PIK3CD, PHOSPHORYLATION AT TYR-552, MUTAGENESIS OF TYR-552.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response."
      Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C.
      Nat. Cell Biol. 12:66-73(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SHIGELLA FLEXNERI IPAH9.8, MUTAGENESIS OF 476-GLU-ARG-477.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: UBIQUITIN-BINDING, MUTAGENESIS OF ASP-472.
    24. "A20, ABIN-1/2, and CARD11 mutations and their prognostic value in gastrointestinal diffuse large B-cell lymphoma."
      Dong G., Chanudet E., Zeng N., Appert A., Chen Y.W., Au W.Y., Hamoudi R.A., Watkins A.J., Ye H., Liu H., Gao Z., Chuang S.S., Srivastava G., Du M.Q.
      Clin. Cancer Res. 17:1440-1451(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TRP-263; MET-286; THR-374 AND LYS-476.

    Entry informationi

    Entry nameiTNIP1_HUMAN
    AccessioniPrimary (citable) accession number: Q15025
    Secondary accession number(s): A4F1W8
    , A4F1W9, A4F1X2, A4F1X4, A4F1X5, A4F1X6, A4F1X7, A4F1X9, B7Z699, E7EPY1, E7ET96, O76008, Q05KP3, Q05KP4, Q6N077, Q96EL9, Q99833, Q9H1J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: August 1, 1999
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3